Kempe M, Mosbach K
Department of Pure and Applied Biochemistry, University of Lund, Sweden.
Int J Pept Protein Res. 1994 Dec;44(6):603-6. doi: 10.1111/j.1399-3011.1994.tb01150.x.
Highly crosslinked synthetic polymers, selective for various N alpha-protected amino acids and derivatives, were prepared by non-covalent molecular imprinting. Methacrylic acid and ethylene glycol dimethacrylate were copolymerized in the presence of the print molecules, which were subsequently extracted from the polymers. The recognition of the polymers for the print molecules and molecules of similar structures was investigated by using the polymers as stationary phases in HPLC. The functional groups of the print molecules interact via hydrogen bonds with the positioned carboxyls of the polymer. It was shown that the N alpha-protecting group, the C alpha-protecting group and the amino acid side chain are also recognized by the binding sites in the polymer.
